Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin

Aneja, Babita; Kumari, Meena; Azam, Amir; Kumar, Amit; Abid, Mohammad; Patel, Rajan

doi:10.1002/bio.3435

Cited by 13 publications

(5 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…When Δλ is 15 nm, the fluorescence intensity of the Tyr residue of BSA did not change regularly with K4 concentration. These results suggested that the conformation of the Trp residue was more affected than Tyr upon BSA– K4 interaction …”

Section: Resultsmentioning

confidence: 85%

Deciphering binding mechanism between bovine serum albumin and new pyrazoline compound K4

Bozkurt

Gül

2019

Luminescence

View full text Add to dashboard Cite

The binding mechanism of a new and possible drug candidate pyrazoline derivative compound K4 and bovine serum albumin (BSA) was investigated in buffer solution (pH 7.4) using ultraviolet-visible light absorption and steady-state and synchronous fluorescence techniques. The fluorescence intensity of BSA was quenched in the presence of K4. The quenching process between BSA and K4 was examined at four different temperatures. Decrease of the quenching constants calculated using the Stern-Volmer equation and at increasing temperature suggested that the interaction BSA-K4 was realized through a static quenching mechanism. Synchronous fluorescence measurements suggested that K4 bounded to BSA at the tryptophan region.Fourier transform infrared spectroscopy results showed that there was no significant change in polarity around the tryptophan residue The forces responsible for the BSA-K4 interaction were examined using thermodynamic parameters. In this study, the calculated negative value of ΔG, the negative value of ΔH and the positive value of ΔS pointed to the interaction being through spontaneous and electrostatic interactions that were dominant for our cases. This study provides a very useful in vitro model to researchers by mimicking in vivo conditions to estimate interactions between a possible drug candidate or a drug and body proteins. K E Y W O R D S bovine serum albumin, fluorescence quenching, FRET, pyrazoline 1 | INTRODUCTION Studies on the interaction between proteins and fluorescent probes are very important as they act as models for biochemical applications in cells. [1-3] Serum albumins are proteins that constitute approximately 60% of total plasma proteins. These proteins play an important role in the transport of exogenous and endogenous substances such as fatty acids, metal ions, drugs, and dyes. Bovine serum albumin (BSA) and human serum albumin (HSA) are proteins that are frequently used in biochemical and biophysical studies. BSA is the 76% structural homologue of HSA. BSA is generally preferred as a model protein due to its ease of use, low cost, stability, and unusual ligand binding properties in laboratory experiments. [4] Spectroscopic techniques such as ultraviolet-visible (UV-vis) light absorption, and steady-state and time-resolved fluorescence measurements are often used to investigate the interactions between BSA or HSA and fluores-cence probes due to their ease of use, accuracy, high precision, and rapid response. [5][6][7] Pyrazoline derivatives are compounds with antimicrobial, [8] antinociceptive, [9] anticancer, [10,11] antidepressant, [12] and anti-inflammatory [13] properties. In addition to the pharmacological importance of these compounds, they are used as fluorescent compounds because of their strong fluorescence properties and high quantum yields. To understand the interaction of these bioactive fluorescent compounds with protein molecules in the cell, studies in the laboratory environment with model systems constitute a marked research area. [14,15] Therefore, it is very importa...

show abstract

Section: Resultsmentioning

confidence: 85%

Deciphering binding mechanism between bovine serum albumin and new pyrazoline compound K4

Bozkurt

Gül

2019

Luminescence

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 98%

“…Obtaining 3D fluorescence data by simultaneously varying both excitation and emission wavelengths across a range offers valuable information about structural changes in the protein. 43 The 3D spectra of BSA and BSA in complexation with gartanin and friedelin are shown in Figure 9 . In Figure 9 A, peak A and peak B arise due to first-order Rayleigh scattering (λ ex = λ em ) and second-order Rayleigh scattering peak (λ ex = 2em), respectively.…”

Section: Resultsmentioning

confidence: 99%

“…It also has a long shelf life and can be easily modified or conjugated with other molecules. In addition, BSA can interact with certain drugs or other compounds, which can affect their pharmacokinetic properties. − Several studies have been done to understand the binding mechanism of ligands with BSA. − …”

Section: Introductionmentioning

confidence: 99%

“… 35 − 37 Several studies have been done to understand the binding mechanism of ligands with BSA. 38 − 43 …”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A Comprehensive Multispectroscopic and Computational Analysis of the Interaction between Plant-Based Antiplasmodial Compounds and Bovine Serum Albumin

Azeem,

Abdulhameed,

Hussain

et al. 2024

ACS Omega

Self Cite

View full text Add to dashboard Cite

This study was conducted to explore the interaction between two plant-based antiplasmodial compounds, gartanin and friedelin, and bovine serum albumin (BSA). The objectives aimed to elucidate the binding characteristics, structural changes, and thermodynamic parameters associated with the interaction. Various methods were used including UV−vis, fluorescence, and circular dichroism spectroscopy, supported by molecular docking and molecular dynamics simulation. The results showed a concentration-dependent interaction between the antiplasmodial compounds and BSA, revealing changes in protein conformation and stability. The obtained results showed that the plant products bound with BSA through static quenching with moderate binding affinity (10 4 M −1 ) with BSA. Thermodynamic parameters and structural transitions calculated from spectroscopic methods revealed that hydrogen bond and van der Waals forces caused the partial conformational alteration in the secondary structure of BSA as the α-helical content decreased with an increase in β sheets, random coils, and other structures. Computational analysis provided insights into the binding sites and affinities. The study enhances our understanding of the molecular interactions between BSA protein and antiplamodial compounds obtained from plants, supporting the research of choosing, designing, and optimizing molecules for biomedical applications with a focus on selectively targeting their binding sites.

show abstract

Biscoumarin–pyrimidine conjugates as potent anticancer agents and binding mechanism of hit candidate with human serum albumin

Reddy

Kongot

Singh

et al. 2020

Archiv der Pharmazie

Self Cite

View full text Add to dashboard Cite

In our continuing efforts to develop therapeutically active coumarin‐based compounds, a series of new C4–C4′ biscoumarin–pyrimidine conjugates (1a–l) was synthesized via SN2 reaction of substituted 4‐bromomethyl coumarin with thymine. All compounds were characterized using spectroscopic techniques, that is, attenuated total reflection infrared (ATR‐IR), CHN elemental analysis, and 1H and 13C NMR (nuclear magnetic resonance). In addition, the structure of compound 1d (1,3‐bis[(7‐chloro‐2‐oxo‐2H‐chromen‐4‐yl)methyl]‐5‐methylpyrimidine‐2,4(1H,3H)‐dione) was established through X‐ray crystallography. Compounds 1a–l were screened for in vitro anticancer activity against C6 rat glioma cells. Among the screened compounds, 1,3‐bis[(6‐chloro‐2‐oxo‐2H‐chromen‐4‐yl)methyl]‐5‐methylpyrimidine‐2,4(1H,3H)‐dione (1c) was identified as the best antiproliferative candidate, exhibiting an IC50 value of 4.85 μM. All the compounds (1a–l) were found to be nontoxic toward healthy human embryonic kidney cells (HEK293), indicating their selective nature. In addition, the most active compound (1c) displayed strong binding interactions with the drug carrier protein, human serum albumin, and exhibited good solution stability at biological pH conditions. Fluorescence, UV–visible spectrophotometry and molecular modeling methodologies were employed for studying the interaction mechanism of compound 1c with protein.

show abstract

Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin

Cited by 13 publications

References 63 publications

Deciphering binding mechanism between bovine serum albumin and new pyrazoline compound K4

Deciphering binding mechanism between bovine serum albumin and new pyrazoline compound K4

A Comprehensive Multispectroscopic and Computational Analysis of the Interaction between Plant-Based Antiplasmodial Compounds and Bovine Serum Albumin

Biscoumarin–pyrimidine conjugates as potent anticancer agents and binding mechanism of hit candidate with human serum albumin

Contact Info

Product

Resources

About